A bacterial homolog to the mitochondrial enoyl-CoA hydratase

Diana L. Beckman; Robert G. Kranz

doi:10.1016/0378-1119(91)90313-Z

A bacterial homolog to the mitochondrial enoyl-CoA hydratase

Diana L. Beckman, Robert G. Kranz

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

A 257-amino acid (aa) open reading frame in the photosynthetic bacterium, Rhodobacter capsulatus, shows significant homology to the mitochondrial enoyl-CoA hydratase (290 aa). This similarity in size and sequence suggests that R. capsulatus oxidizes fatty acids using specific components, more like the mitochondrial system than the multifunctional component system of Escherichia coli.

Original language	English
Pages (from-to)	171-172
Number of pages	2
Journal	Gene
Volume	107
Issue number	1
DOIs	https://doi.org/10.1016/0378-1119(91)90313-Z
State	Published - Oct 30 1991

Keywords

(Fatty-acid metabolism
Rhodobacter capsulatus
peroxisome
recombinant DNA)

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10.1016/0378-1119(91)90313-Z

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title = "A bacterial homolog to the mitochondrial enoyl-CoA hydratase",

abstract = "A 257-amino acid (aa) open reading frame in the photosynthetic bacterium, Rhodobacter capsulatus, shows significant homology to the mitochondrial enoyl-CoA hydratase (290 aa). This similarity in size and sequence suggests that R. capsulatus oxidizes fatty acids using specific components, more like the mitochondrial system than the multifunctional component system of Escherichia coli.",

keywords = "(Fatty-acid metabolism, Rhodobacter capsulatus, peroxisome, recombinant DNA)",

author = "Beckman, {Diana L.} and Kranz, {Robert G.}",

note = "Funding Information: R.G.K. is supported by NIH FIRST Grant GM 39106, BRSGS07 RR077054 and the Markey Center in the Molecular Biology of Human Disease.",

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AU - Beckman, Diana L.

AU - Kranz, Robert G.

N1 - Funding Information: R.G.K. is supported by NIH FIRST Grant GM 39106, BRSGS07 RR077054 and the Markey Center in the Molecular Biology of Human Disease.

PY - 1991/10/30

Y1 - 1991/10/30

N2 - A 257-amino acid (aa) open reading frame in the photosynthetic bacterium, Rhodobacter capsulatus, shows significant homology to the mitochondrial enoyl-CoA hydratase (290 aa). This similarity in size and sequence suggests that R. capsulatus oxidizes fatty acids using specific components, more like the mitochondrial system than the multifunctional component system of Escherichia coli.

AB - A 257-amino acid (aa) open reading frame in the photosynthetic bacterium, Rhodobacter capsulatus, shows significant homology to the mitochondrial enoyl-CoA hydratase (290 aa). This similarity in size and sequence suggests that R. capsulatus oxidizes fatty acids using specific components, more like the mitochondrial system than the multifunctional component system of Escherichia coli.

KW - (Fatty-acid metabolism

KW - Rhodobacter capsulatus

KW - peroxisome

KW - recombinant DNA)

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U2 - 10.1016/0378-1119(91)90313-Z

DO - 10.1016/0378-1119(91)90313-Z

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SN - 0378-1119

VL - 107

SP - 171

EP - 172

JO - Gene

JF - Gene

IS - 1

ER -

A bacterial homolog to the mitochondrial enoyl-CoA hydratase

Abstract

Keywords

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